DSG1_CANLF
ID DSG1_CANLF Reviewed; 1054 AA.
AC Q9GKQ8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Desmoglein-1;
DE AltName: Full=Desmosomal glycoprotein 1;
DE Short=DG1;
DE Short=DGI;
DE Flags: Precursor;
GN Name=DSG1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lip;
RX PubMed=10844571; DOI=10.1046/j.1523-1747.2000.00005-4.x;
RA Muller E., Caldelari R., Levine R., Kaplan S., Baron A., Rohrbach B.,
RA Wyder M., Balmer V., Suter M.M.;
RT "Cloning of canine Dsg1 and evidence for alternative polyadenylation.";
RL J. Invest. Dermatol. 114:1211-1213(2000).
CC -!- FUNCTION: Component of intercellular desmosome junctions. Involved in
CC the interaction of plaque proteins and intermediate filaments mediating
CC cell-cell adhesion (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to JUP/plakoglobin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cell junction, desmosome {ECO:0000250}.
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC cadherin domain and rigidify the connections, imparting a strong
CC curvature to the full-length ectodomain. {ECO:0000250}.
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DR EMBL; AF005360; AAD01241.1; -; mRNA.
DR RefSeq; NP_001002939.1; NM_001002939.1.
DR AlphaFoldDB; Q9GKQ8; -.
DR SMR; Q9GKQ8; -.
DR STRING; 9612.ENSCAFP00000031230; -.
DR PaxDb; Q9GKQ8; -.
DR PRIDE; Q9GKQ8; -.
DR GeneID; 403401; -.
DR KEGG; cfa:403401; -.
DR CTD; 1828; -.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; Q9GKQ8; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0030057; C:desmosome; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0045295; F:gamma-catenin binding; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR Gene3D; 4.10.900.10; -; 1.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR InterPro; IPR027397; Catenin-bd_sf.
DR InterPro; IPR009123; Desmoglein.
DR InterPro; IPR009122; Desmosomal_cadherin.
DR Pfam; PF00028; Cadherin; 3.
DR Pfam; PF01049; Cadherin_C; 1.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR01818; DESMOCADHERN.
DR PRINTS; PR01819; DESMOGLEIN.
DR SMART; SM00112; CA; 4.
DR SUPFAM; SSF49313; SSF49313; 4.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 4.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell junction; Cell membrane;
KW Cleavage on pair of basic residues; Glycoprotein; Membrane; Metal-binding;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..49
FT /evidence="ECO:0000255"
FT /id="PRO_0000003835"
FT CHAIN 50..1054
FT /note="Desmoglein-1"
FT /id="PRO_0000003836"
FT TOPO_DOM 50..566
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 567..587
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 588..1054
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 50..157
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 158..269
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 270..389
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 386..493
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REPEAT 830..856
FT /note="Desmoglein repeat 1"
FT REPEAT 857..886
FT /note="Desmoglein repeat 2"
FT REPEAT 887..916
FT /note="Desmoglein repeat 3"
FT REPEAT 917..944
FT /note="Desmoglein repeat 4"
FT REPEAT 945..973
FT /note="Desmoglein repeat 5"
FT REGION 487..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1018..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1054 AA; 113857 MW; B86B90F48EE5F303 CRC64;
MNWHFLRTAT VLLIFLVVVE INSEFRIQVR DYNTKNGTIK WHSIRRQKRE WIKFAAACRE
GEDNSKRNPI AKIHSDCAAN QQVTYRISGV GIDQPPYGIF IINQKTGEIN ITSIVDREIT
PFFIIYCRAL NSLGQDLERP LELRVRVLDI NDNPPVFSMS TFVGQIEENS NANTLVMRLN
ATGADEPNNL NSKIAFKIIR QEPSDSPMFI INRNTGEIRT MNNFLDREQY SQYSLAVRGS
DRDGGADGMS AECECNIKIL DVNDNIPYME PSSHMVRIEE NALSQNLVEI RVIDLDEEFS
ANWMAVIFFI SGNEGGWFDI EMNERTNVGI LKVIKPLDYE AVQNLQLSLG VRNKADFHHS
IMSQYKVTAT AISVTVLNVI EGSVFRPGSK TYVVRSDMGQ NYKVGDFVAT DLDTGLASTT
VRYVMGNNPA NLLNVDSKTG VITLRNKVTM EQYEMLNGKY QGTILSIDDA LQRTCTGTIN
IDLQGSGWEK DSEKVTSSQN SGSSTGDSSG GTGGGGRENP SEGDTTTNTG GKTSTDYEDG
ETQTQSNNNH QELGSNNLSD NVHFGPAGIG LLIMGFLVLG LVPFLLMCCD CGGAPGAGAG
FEPVPECSDG AIHSWAVEGP QPLPTDATTV CVPPIPSNNA NVIECIDTSG VYTNEYGGRE
MQDLGGGERT TGFELTEGVK TSGVPEICQE YSGTLRRNSM RECREGGLNM NFMESYFCQK
AYAYADEDEG RPSNDCLLIY DIEGVGSPAG SVGCCSFIGE DLDDSFLDTL GPKFKKLADI
SLGKEVEPDP SWPPESTEPI CPQQGTEPII GGHPPISPHF GTTTVISENT YPSGPGVQHP
MPIPDPLGYG NVTVTESYTT SGTLKPTVHV HDNRHASNVV VTERVVGPIS GTDLHGMLEM
PDLRDGSNVI VTERVIAPSS SLPTSLTMPD PRESSNVVVT ERVIRPASGM MGNLSIHPEL
SNAQNVIVTE RVVSGSGISG ISGLVGSAMG VSGGGMAMNS LGGGGGLSSS MGGTATIGHV
RSSSDHHFSQ TLGSASPSTA RSRITKYSTV QYTK
